Journal
JOURNAL OF MASS SPECTROMETRY
Volume 46, Issue 8, Pages 742-750Publisher
WILEY
DOI: 10.1002/jms.1951
Keywords
cross-linking; peptide fragmentation; mass spectrometry; protein structure; MALDI; ESI
Funding
- Sao Paulo Proteome Network [FAPESP 2004/14846-0, FINEP 01.07.0290.00]
- Instituto Nacional de Ciencia e Tecnologia de Bioanalitica [CNPq 573672/2008-3, FAPESP 08/57805-2]
- FAPESP [2007/55930-1]
- CAPES
- CNPq
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The use of mass spectrometry coupled with chemical cross-linking of proteins has become one of the most useful tools for proteins structure and interactions studies. One of the challenges in these studies is the identification of the cross-linked peptides. The interpretation of the MS/MS data generated in cross-linking experiments using N-hydroxy succinimide esters is not trivial once a new amide bond is formed allowing new fragmentation pathways, unlike linear peptides. Intermolecular cross-linked peptides occur when two different peptides are connected by the cross-linker and they yield information on the spatial proximity of different domains (within a protein) or proteins (within a complex). In this article, we report a detailed fragmentation study of intermolecular cross-linked peptides, generated from a set of synthetic peptides, using both ESI and MAID! to generate the precursor ions. The fragmentation features observed here can be helpful in the interpretation and identification of cross-linked peptides present in cross-linking experiments and be further implemented in search engine's algorithms. Copyright (C) 2011 John Wiley & Sons, Ltd.
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